BMRB Entry 17804

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR17804

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Title:
1H, 15N and 13C backbone resonance assignments of alpha1-antitrypsin
Deposition date:
2011-07-25
Original release date:
2011-11-30
Authors:
Nyon, Mun Peak; Kirkpatrick, John; Cabrita, Lisa; Christodoulou, John; Gooptu, Bibek
Citation:

Citation: Nyon, Mun Peak; Kirkpatrick, John; Cabrita, Lisa; Christodoulou, John; Gooptu, Bibek. "1H, 15N and 13C backbone resonance assignments of the archetypal serpin 1-antitrypsin."  Biomol. NMR Assignments 6, 153-156 (2012).
PubMed: 22109101

Assembly members:

Assembly members:
AAT, polymer, 404 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pQE31

Entity Sequences (FASTA):

Entity Sequences (FASTA):
AAT: MRGSHHHHHHTDPQGDAAQK TDTSHHDQDHPTFNKITPNL AEFAFSLYRQLAHQSNSTNI FFSPVSIATAFAMLSLGTKA DTHDEILEGLNFNLTEIPEA QIHEGFQELLRTLNQPDSQL QLTTGNGLFLSEGLKLVDKF LEDVKKLYHSEAFTVNFGDT EEAKKQINDYVEKGTQGKIV DLVKELDRDTVFALVNYIFF KGKWERPFEVKDTEEEDFHV DQVTTVKVPMMKRLGMFNIQ HCKKLSSWVLLMKYLGNATA IFFLPDEGKLQHLENELTHD IITKFLENEDRRSASLHLPK LSITGTYDLKSVLGQLGITK VFSNGADLSGVTEEAPLKLS KAVHKAVLTIDEKGTEAAGA MFLEAIPMSIPPEVKFNKPF VFLMIEQNTKSPLFMGKVVN PTQK

Data sets:
Data typeCount
13C chemical shifts1287
15N chemical shifts616
1H chemical shifts616

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1AAT1

Entities:

Entity 1, AAT 404 residues - Formula weight is not available

1   METARGGLYSERHISHISHISHISHISHIS
2   THRASPPROGLNGLYASPALAALAGLNLYS
3   THRASPTHRSERHISHISASPGLNASPHIS
4   PROTHRPHEASNLYSILETHRPROASNLEU
5   ALAGLUPHEALAPHESERLEUTYRARGGLN
6   LEUALAHISGLNSERASNSERTHRASNILE
7   PHEPHESERPROVALSERILEALATHRALA
8   PHEALAMETLEUSERLEUGLYTHRLYSALA
9   ASPTHRHISASPGLUILELEUGLUGLYLEU
10   ASNPHEASNLEUTHRGLUILEPROGLUALA
11   GLNILEHISGLUGLYPHEGLNGLULEULEU
12   ARGTHRLEUASNGLNPROASPSERGLNLEU
13   GLNLEUTHRTHRGLYASNGLYLEUPHELEU
14   SERGLUGLYLEULYSLEUVALASPLYSPHE
15   LEUGLUASPVALLYSLYSLEUTYRHISSER
16   GLUALAPHETHRVALASNPHEGLYASPTHR
17   GLUGLUALALYSLYSGLNILEASNASPTYR
18   VALGLULYSGLYTHRGLNGLYLYSILEVAL
19   ASPLEUVALLYSGLULEUASPARGASPTHR
20   VALPHEALALEUVALASNTYRILEPHEPHE
21   LYSGLYLYSTRPGLUARGPROPHEGLUVAL
22   LYSASPTHRGLUGLUGLUASPPHEHISVAL
23   ASPGLNVALTHRTHRVALLYSVALPROMET
24   METLYSARGLEUGLYMETPHEASNILEGLN
25   HISCYSLYSLYSLEUSERSERTRPVALLEU
26   LEUMETLYSTYRLEUGLYASNALATHRALA
27   ILEPHEPHELEUPROASPGLUGLYLYSLEU
28   GLNHISLEUGLUASNGLULEUTHRHISASP
29   ILEILETHRLYSPHELEUGLUASNGLUASP
30   ARGARGSERALASERLEUHISLEUPROLYS
31   LEUSERILETHRGLYTHRTYRASPLEULYS
32   SERVALLEUGLYGLNLEUGLYILETHRLYS
33   VALPHESERASNGLYALAASPLEUSERGLY
34   VALTHRGLUGLUALAPROLEULYSLEUSER
35   LYSALAVALHISLYSALAVALLEUTHRILE
36   ASPGLULYSGLYTHRGLUALAALAGLYALA
37   METPHELEUGLUALAILEPROMETSERILE
38   PROPROGLUVALLYSPHEASNLYSPROPHE
39   VALPHELEUMETILEGLUGLNASNTHRLYS
40   SERPROLEUPHEMETGLYLYSVALVALASN
41   PROTHRGLNLYS

Samples:

sample_1: AAT, [U-100% 13C; U-100% 15N; U-80% 2H], 0.225 ± 0.025 mM; sodium phosphate 25 mM; sodium chloride 50 mM; EDTA 1 mM; DSS 0.001%; H2O 90%; D2O 10%

sample_2: AAT, [U-100% 13C; U-100% 15N; U-80% 2H], 0.225 ± 0.050 mM; sodium phosphate 25 mM; sodium chloride 50 mM; EDTA 1 mM; DSS 0.001%; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.1 M; pH: 8.0; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 0.1 M; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_2
3D HNCAsample_2isotropicsample_conditions_2

Software:

TOPSPIN v2.1.6, Bruker Biospin - collection

AZARA v2.8, Boucher - processing

VNMRJ v2.2D, Varian - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

ANALYSIS v2.2, CCPN - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Varian INOVA 600 MHz
  • Varian INOVA 800 MHz
  • Varian INOVA 900 MHz

Related Database Links:

PDB
DBJ BAG38005 BAI45729
EMBL CAA25838 CAD61914 CAD62306 CAD62334 CAD62585
GB AAA51546 AAA51547 AAB59375 AAB59495 AAF29581
PRF 1012287A
REF NP_000286 NP_001002235 NP_001002236 NP_001121172 NP_001121173
SP P01009
AlphaFold P01009

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks